生物
阿尔戈瑙特
嗜热菌
核酸
计算生物学
核酸内切酶
DNA
劈理(地质)
细胞生物学
遗传学
基因
核糖核酸
RNA干扰
断裂(地质)
古生物学
大肠杆菌
作者
Benjamin Ober-Reynolds,Winston R. Becker,Karina Jouravleva,Samson M. Jolly,Phillip D. Zamore,William J. Greenleaf
出处
期刊:Molecular Cell
[Elsevier]
日期:2022-04-01
卷期号:82 (7): 1329-1342.e8
被引量:8
标识
DOI:10.1016/j.molcel.2022.02.026
摘要
Argonautes are nucleic acid-guided proteins that perform numerous cellular functions across all domains of life. Little is known about how distinct evolutionary pressures have shaped each Argonaute’s biophysical properties. We applied high-throughput biochemistry to characterize how Thermus thermophilus Argonaute (TtAgo), a DNA-guided DNA endonuclease, finds, binds, and cleaves its targets. We found that TtAgo uses biophysical adaptations similar to those of eukaryotic Argonautes for rapid association but requires more extensive complementarity to achieve high-affinity target binding. Using these data, we constructed models for TtAgo association rates and equilibrium binding affinities that estimate the nucleic acid- and protein-mediated components of the target interaction energies. Finally, we showed that TtAgo cleavage rates vary widely based on the DNA guide, suggesting that only a subset of guides cleaves targets on physiologically relevant timescales.
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